ID A0A091JTD9_COLST Unreviewed; 937 AA.
AC A0A091JTD9;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=Beta-1,4-N-acetylgalactosaminyltransferase {ECO:0000256|RuleBase:RU364016};
DE EC=2.4.1.244 {ECO:0000256|RuleBase:RU364016};
DE Flags: Fragment;
GN ORFNames=N325_00901 {ECO:0000313|EMBL:KFP28422.1};
OS Colius striatus (Speckled mousebird).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Coliiformes; Coliidae; Colius.
OX NCBI_TaxID=57412 {ECO:0000313|EMBL:KFP28422.1, ECO:0000313|Proteomes:UP000053615};
RN [1] {ECO:0000313|EMBL:KFP28422.1, ECO:0000313|Proteomes:UP000053615}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N325 {ECO:0000313|EMBL:KFP28422.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Transfers N-acetylgalactosamine (GalNAc) from UDP-GalNAc to
CC N-acetylglucosamine-beta-benzyl with a beta-1,4-linkage to form N,N'-
CC diacetyllactosediamine, GalNAc-beta-1,4-GlcNAc structures in N-linked
CC glycans and probably O-linked glycans. {ECO:0000256|RuleBase:RU364016}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an N-acetyl-beta-D-glucosaminyl derivative + UDP-N-acetyl-
CC alpha-D-galactosamine = an N-acetyl-beta-D-galactosaminyl-(1->4)-N-
CC acetyl-beta-D-glucosaminyl derivative + H(+) + UDP;
CC Xref=Rhea:RHEA:20493, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:61631, ChEBI:CHEBI:67138, ChEBI:CHEBI:138027;
CC EC=2.4.1.244; Evidence={ECO:0000256|RuleBase:RU364016};
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane
CC {ECO:0000256|RuleBase:RU364016}; Single-pass type II membrane protein
CC {ECO:0000256|RuleBase:RU364016}. Membrane
CC {ECO:0000256|ARBA:ARBA00004606}; Single-pass type II membrane protein
CC {ECO:0000256|ARBA:ARBA00004606}.
CC -!- SIMILARITY: Belongs to the chondroitin N-
CC acetylgalactosaminyltransferase family. {ECO:0000256|ARBA:ARBA00009239,
CC ECO:0000256|RuleBase:RU364016}.
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DR EMBL; KK532387; KFP28422.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091JTD9; -.
DR Proteomes; UP000053615; Unassembled WGS sequence.
DR GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0033842; F:N-acetyl-beta-glucosaminyl-glycoprotein 4-beta-N-acetylgalactosaminyltransferase activity; IEA:UniProtKB-EC.
DR InterPro; IPR008428; Chond_GalNAc.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR InterPro; IPR037524; PA14/GLEYA.
DR InterPro; IPR011658; PA14_dom.
DR PANTHER; PTHR12369:SF15; BETA-1,4-N-ACETYLGALACTOSAMINYLTRANSFERASE 3; 1.
DR PANTHER; PTHR12369; CHONDROITIN SYNTHASE; 1.
DR Pfam; PF05679; CHGN; 1.
DR Pfam; PF07691; PA14; 1.
DR SMART; SM00758; PA14; 1.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
DR PROSITE; PS51820; PA14; 1.
PE 3: Inferred from homology;
KW Golgi apparatus {ECO:0000256|RuleBase:RU364016};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000053615};
KW Signal-anchor {ECO:0000256|RuleBase:RU364016};
KW Transferase {ECO:0000256|RuleBase:RU364016, ECO:0000313|EMBL:KFP28422.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 60..222
FT /note="PA14"
FT /evidence="ECO:0000259|PROSITE:PS51820"
FT REGION 246..269
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 432..463
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 525..568
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 441..455
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 552..568
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFP28422.1"
FT NON_TER 937
FT /evidence="ECO:0000313|EMBL:KFP28422.1"
SQ SEQUENCE 937 AA; 107465 MW; 4B904A0A85C45618 CRC64;
YESWRDLAKA LADTNVPGGD ASLQFYYLKK LRHQNQELQR DGRNKSNYAA VDNPVRWIPE
FQGQANLHVF EDWCGNSIEQ LRKNLHFPLF PHTRTTLKKL AVSPKWTNYG LRIFGYLHPF
TNGEFQFAIA ADDNAEFWLS PDEKTSGLQL LASVGKTGKE WTAPGEFGKF HSQQSKTVRL
SATGRYYFEV LHKQDDRGTD HVEVAWRLND PEAKFKVIDS QYLSLFANET LLKMNEVGHI
PQTLASHTRR PADSAGGQAH PADMLKPDPR DTLYKVPLLN KSRVRRALPD CLYKPSYLVN
GFPLQRYQGL QFVHLSFVYP NDYSRLTHME KDNKCFYQEN SYYLERFGFY KYMKMDRPEK
SLDSGEKTEQ PGAKEADTIE GTAPVCGSIP VPLSRSDNAE MRQEAAFPPA AGQAPGLGRG
RQEDEARGVT AVCPAGSQEG NVEELQYTEQ DTESPSAPEH GGMGRAELAA NTLSSLLGSE
NIHQDYSFRE RRSLRRVVGT ASPSQQPGLP QWLNQVESYI AEQKAANGGH RAKGEAQVVS
PMKGKSGPVA AEEEEEEADG EAEEEDEEDF DYVPVFDQAV NWEQTFSISN LDFHMLRTDW
IDLKCNTSGN LLLKEREALE ITRVFLKKLN QRSKGRFQLQ RIVNVEKRQD RMRGSRYLLE
LELLEQGERL VRFSEYIFAQ GWQGIDGDEE EERKMRNLAW GRRRHLMAVA NEPELCWPQG
FSWNHRAVVH FVVPVKNQAR WVLQFISDME ELFRVTKDPY FNVIITDYSS DDMDVEKAMK
RSTLHSYRYL KLTGNFERSA GLQAGIDLVT DPHSIIFLCD LHIHFPAGVI DSIRKHCVEG
KMAFAPMVMR LHCGMSPQRP DGYWEVNGFG LLGIYKSDLD RIGGMNTKEF RDRWGGEDWE
LLDRILQAGL EVERLSLRNF FHWFHSKRGM WNRRQLK
//
